메뉴 건너뛰기




Volumn 90, Issue 3, 2004, Pages 585-594

Examination of the rate of peptide biosynthesis in neuroendocrine cell lines using a stable isotopic label and mass spectrometry

Author keywords

Carboxypeptidase; Gamma lipotropin; Insulin; Prohormone convertase; Proinsulin; Proopiomelanocortin

Indexed keywords

CHLOROQUINE; CONVERTASE 1; DEUTERIUM; FORSKOLIN; GAMMA LIPOTROPIN; HORMONE PRECURSOR; INSULIN; LEUCINE; LIPOTROPIN; PEPTIDE; POTASSIUM CHLORIDE; PROSERYLALANYLALANYLSERINE; UNCLASSIFIED DRUG;

EID: 3343013767     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02522.x     Document Type: Article
Times cited : (15)

References (44)
  • 1
    • 0037023692 scopus 로고    scopus 로고
    • Mitochondrial metabolism sets the maximal limit of fuel-stimulated insulin secretion in a model pancreatic beta cell: A survey of four fuel secretagogues
    • Antinozzi P. A., Ishihara H., Newgard C. B. and Wollheim C. B. (2002) Mitochondrial metabolism sets the maximal limit of fuel-stimulated insulin secretion in a model pancreatic beta cell: a survey of four fuel secretagogues. J. Biol. Chem. 277, 11746-11755.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11746-11755
    • Antinozzi, P.A.1    Ishihara, H.2    Newgard, C.B.3    Wollheim, C.B.4
  • 2
    • 0026550830 scopus 로고
    • Establishment of 2-mercaptoethanol-dependent differentiated insulin-secreting cell lines
    • Asfari M., Janjic D., Meda P., Li G., Halban P. A. and Wollheim C. B. (1992) Establishment of 2-mercaptoethanol-dependent differentiated insulin-secreting cell lines. Endocrinology 130, 167-178.
    • (1992) Endocrinology , vol.130 , pp. 167-178
    • Asfari, M.1    Janjic, D.2    Meda, P.3    Li, G.4    Halban, P.A.5    Wollheim, C.B.6
  • 3
    • 0034640505 scopus 로고    scopus 로고
    • The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1
    • Cameron A., Fortenberry Y. and Lindberg I. (2000) The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1. FEBS Lett. 473, 135-138.
    • (2000) FEBS Lett. , vol.473 , pp. 135-138
    • Cameron, A.1    Fortenberry, Y.2    Lindberg, I.3
  • 4
    • 0036645730 scopus 로고    scopus 로고
    • fat mice using differential isotopic tags and mass spectrometry
    • fat mice using differential isotopic tags and mass spectrometry. Anal Chem. 74, 3190-3198.
    • (2002) Anal. Chem. , vol.74 , pp. 3190-3198
    • Che, F.-Y.1    Fricker, L.D.2
  • 8
    • 0025821271 scopus 로고
    • Peptidyl-α-hydroxyglycine α-amidating lyase: Purification, characterization, and expression
    • Eipper B. A., Perkins S. N., Husten E. J., Johnson R. C., Keutmann H. T. and Mains R. E. (1991) Peptidyl-α-hydroxyglycine α-amidating lyase: Purification, characterization, and expression. J. Biol. Chem. 266, 7827-7833.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7827-7833
    • Eipper, B.A.1    Perkins, S.N.2    Husten, E.J.3    Johnson, R.C.4    Keutmann, H.T.5    Mains, R.E.6
  • 9
    • 0037085361 scopus 로고    scopus 로고
    • Functional characterization of ProSAAS: Similarities and differences with 7B2
    • Fortenberry Y., Hwang J. R., Apletalina E. V. and Lindberg I. (2002) Functional characterization of ProSAAS: similarities and differences with 7B2. J. Biol. Chem. 277, 5175-5186.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5175-5186
    • Fortenberry, Y.1    Hwang, J.R.2    Apletalina, E.V.3    Lindberg, I.4
  • 10
    • 0001912912 scopus 로고    scopus 로고
    • Carboxypeptidase E/H
    • (Barrett, A., J. Rawlings, N. D. and Woessner, J. and F., eds). Academic Press, San Diego
    • Fricker L. D. (1998) Carboxypeptidase E/H, in Handbook of Proteolytic Enzymes (Barrett, A., J. Rawlings, N. D. and Woessner, J. and F., eds), pp. 1341-1344. Academic Press, San Diego.
    • (1998) Handbook of Proteolytic Enzymes , pp. 1341-1344
    • Fricker, L.D.1
  • 11
    • 77956702352 scopus 로고    scopus 로고
    • Carboxypeptidases E and D
    • (Dalbey, R. E. and Sigman, D. S., eds). Academic Press, San Diego
    • Fricker L. D. (2002) Carboxypeptidases E and D, in The Enzymes: Co- and Posttranslational Proteolysis of Proteins, Vol. 23 (Dalbey, R. E. and Sigman, D. S., eds), pp. 421-452. Academic Press, San Diego.
    • (2002) The Enzymes: Co- and Posttranslational Proteolysis of Proteins , vol.23 , pp. 421-452
    • Fricker, L.D.1
  • 12
    • 0001727492 scopus 로고
    • Enkephalin convertase: Purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules
    • Fricker L. D. and Snyder S. H. (1982) Enkephalin convertase: purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules. Proc. Natl Acad. Sci. USA 79, 3886-3890.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 3886-3890
    • Fricker, L.D.1    Snyder, S.H.2
  • 13
    • 0034651077 scopus 로고    scopus 로고
    • Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing
    • Fricker L. D., McKinzie A. A, Sun J. et al. (2000) Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing. J. Neurosci. 20, 639-648.
    • (2000) J. Neurosci. , vol.20 , pp. 639-648
    • Fricker, L.D.1    McKinzie, A.A.2    Sun, J.3
  • 14
    • 0034662190 scopus 로고    scopus 로고
    • Detection and quantification of neurotensin in human brain tissue by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Gobom J., Kraeuter K., Persson R., Steen H., Roepstorff P. and Ekman R. (2000) Detection and quantification of neurotensin in human brain tissue by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Chem. 72, 3320-3326.
    • (2000) Anal. Chem. , vol.72 , pp. 3320-3326
    • Gobom, J.1    Kraeuter, K.2    Persson, R.3    Steen, H.4    Roepstorff, P.5    Ekman, R.6
  • 15
    • 0019971028 scopus 로고
    • Evidence that glucose 'marks' beta cells resulting in preferential release of newly synthesized insulin
    • Gold G., Gishizky M. L. and Grodsky G. M. (1982a) Evidence that glucose 'marks' beta cells resulting in preferential release of newly synthesized insulin. Science 218, 56-58.
    • (1982) Science , vol.218 , pp. 56-58
    • Gold, G.1    Gishizky, M.L.2    Grodsky, G.M.3
  • 16
    • 0020062977 scopus 로고
    • Heterogeneity and compartmental properties of insulin storage and secretion in rat islets
    • Gold G., Landahl H. D., Gishizky M. L. and Grodsky G. M. (1982b) Heterogeneity and compartmental properties of insulin storage and secretion in rat islets. J. Clin. Invest. 69, 554-563.
    • (1982) J. Clin. Invest. , vol.69 , pp. 554-563
    • Gold, G.1    Landahl, H.D.2    Gishizky, M.L.3    Grodsky, G.M.4
  • 17
    • 0037307837 scopus 로고    scopus 로고
    • Stable isotope-coded proteomic mass spectrometry
    • Goshe M. B. and Smith R. D. (2003) Stable isotope-coded proteomic mass spectrometry. Curr. Opin. Biotechnol. 14, 101-109.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 101-109
    • Goshe, M.B.1    Smith, R.D.2
  • 18
    • 0026742381 scopus 로고
    • Regulation of carboxypeptidase E: Effect of pH, temperature and Co++ on kinetic parameters of substrate hydrolysis
    • Greene D., Das B. and Fricker L. D. (1992) Regulation of carboxypeptidase E: effect of pH, temperature and Co++ on kinetic parameters of substrate hydrolysis. Biochem. J. 285, 613-618.
    • (1992) Biochem. J. , vol.285 , pp. 613-618
    • Greene, D.1    Das, B.2    Fricker, L.D.3
  • 19
    • 0037270746 scopus 로고    scopus 로고
    • Precise peptide sequencing and protein quantification in the human proteome through in vivo lysine-specific mass tagging
    • Gu S., Pan S., Bradbury E. M. and Chen X. (2003) Precise peptide sequencing and protein quantification in the human proteome through in vivo lysine-specific mass tagging. J. Am. Soc. Mass Spectrom. 14, 1-7.
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 1-7
    • Gu, S.1    Pan, S.2    Bradbury, E.M.3    Chen, X.4
  • 20
    • 37049064057 scopus 로고
    • Secretion of newly synthesized insulin in vitro
    • Howell S. L., Parry D. G. and Taylor K. W. (1965) Secretion of newly synthesized insulin in vitro. Nature 208, 487.
    • (1965) Nature , vol.208 , pp. 487
    • Howell, S.L.1    Parry, D.G.2    Taylor, K.W.3
  • 21
    • 12644256625 scopus 로고    scopus 로고
    • Pattern changes of pituitary peptides in rat after salt-loading as dected by means of direct, semiquantitative mass spectrometric profiling
    • Jimenez C. R., Li K. W., Dreisewerd K. et al. (1997) Pattern changes of pituitary peptides in rat after salt-loading as dected by means of direct, semiquantitative mass spectrometric profiling. Proc. Natl Acad. Sci. USA 94, 9481-9486.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9481-9486
    • Jimenez, C.R.1    Li, K.W.2    Dreisewerd, K.3
  • 22
    • 0036499999 scopus 로고    scopus 로고
    • Quantifying peptides in isotopically labeled protease digests by ion mobility/time-of-flight mass spectrometry
    • Kindy J. M., Taraszka J. A., Regnier F. E. and Clemmer D. E. (2002) Quantifying peptides in isotopically labeled protease digests by ion mobility/time-of-flight mass spectrometry. Anal. Chem. 74, 950-958.
    • (2002) Anal. Chem. , vol.74 , pp. 950-958
    • Kindy, J.M.1    Taraszka, J.A.2    Regnier, F.E.3    Clemmer, D.E.4
  • 24
    • 0024278677 scopus 로고
    • The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin
    • Mains R. E. and May V. (1988) The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin. J. Biol. Chem. 263, 7887-7894.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7887-7894
    • Mains, R.E.1    May, V.2
  • 26
    • 0020684553 scopus 로고
    • Chloroquin diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells
    • Moore H. P., Gumbiner B. and Kelly R. B. (1983) Chloroquin diverts ACTH from a regulated to a constitutive secretory pathway in AtT-20 cells. Nature (Lond.) 302, 434-436.
    • (1983) Nature (Lond.) , vol.302 , pp. 434-436
    • Moore, H.P.1    Gumbiner, B.2    Kelly, R.B.3
  • 27
    • 0025990079 scopus 로고
    • The ordered secretion of bioactive peptides: Oldest or newest first?
    • Noel G. and Mains R. E. (1991) The ordered secretion of bioactive peptides: oldest or newest first? Mol. Endocrinol. 5, 787-794.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 787-794
    • Noel, G.1    Mains, R.E.2
  • 28
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S. E., Blagoev B., Kratchmarova I., Kristensen D. B., Steen H., Pandey A. and Mann M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1, 376-386.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 29
    • 0022979193 scopus 로고
    • Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles
    • Orci L., Ravazzola M., Amherdt M., Madsen O., Perrelet A., Vassalli J. D. and Anderson R. G. (1986) Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles. J. Cell Biol. 103, 2273-2281.
    • (1986) J. Cell Biol. , vol.103 , pp. 2273-2281
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Perrelet, A.5    Vassalli, J.D.6    Anderson, R.G.7
  • 30
    • 0023610730 scopus 로고
    • Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated vesicles
    • Orci L., Ravazzola M., Storch M. J., Anderson R. G. W., Vassalli J. D. and Perrelet A. (1987) Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated vesicles. Cell 49, 865-868.
    • (1987) Cell , vol.49 , pp. 865-868
    • Orci, L.1    Ravazzola, M.2    Storch, M.J.3    Anderson, R.G.W.4    Vassalli, J.D.5    Perrelet, A.6
  • 32
    • 18344389894 scopus 로고    scopus 로고
    • Stable isotope labelling in vivo as an aid to protein identification in peptide mass fingerprinting
    • Pratt J. M., Robertson D. H., Gaskell S. J. et al. (2002b) Stable isotope labelling in vivo as an aid to protein identification in peptide mass fingerprinting. Proteomics 2, 157-163,
    • (2002) Proteomics , vol.2 , pp. 157-163
    • Pratt, J.M.1    Robertson, D.H.2    Gaskell, S.J.3
  • 33
    • 0034604618 scopus 로고    scopus 로고
    • The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1
    • Qian Y., Devi L. A., Mzhavia N., Munzer S., Seidah N. G. and Fricker L. D. (2000) The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1. J. Biol. Chem. 275, 23596-23601.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23596-23601
    • Qian, Y.1    Devi, L.A.2    Mzhavia, N.3    Munzer, S.4    Seidah, N.G.5    Fricker, L.D.6
  • 34
    • 0015351852 scopus 로고
    • Studies on the secretion of newly synthesized proinsulin and insulin from isolated rat islets of Langerhans
    • Sando H., Borg J. and Steiner D. F. (1972) Studies on the secretion of newly synthesized proinsulin and insulin from isolated rat islets of Langerhans. J. Clin. Invest 51, 1476-1485.
    • (1972) J. Clin. Invest. , vol.51 , pp. 1476-1485
    • Sando, H.1    Borg, J.2    Steiner, D.F.3
  • 35
    • 0002652573 scopus 로고    scopus 로고
    • Peptidomics technologies for human body fluids
    • Schrader M. and Schulz-Knappe P. (2001) Peptidomics technologies for human body fluids. Trends Biotechnol. 19, S55-S60.
    • (2001) Trends Biotechnol. , vol.19
    • Schrader, M.1    Schulz-Knappe, P.2
  • 36
    • 0001902818 scopus 로고    scopus 로고
    • Prohormone Convertase 2
    • (Barrett, A. J., Rawlings, N. D. and Woessner, J. F., eds). Academic Press, San Diego
    • Seidah N. G. and Chretien M. (1998a) Prohormone Convertase 2, in Handbook of Proteolytic Enzymes (Barrett, A. J., Rawlings, N. D. and Woessner, J. F., eds), pp. 345-357. Academic Press, San Diego.
    • (1998) Handbook of Proteolytic Enzymes , pp. 345-357
    • Seidah, N.G.1    Chretien, M.2
  • 37
    • 0001809893 scopus 로고    scopus 로고
    • Proprotein Convertase I
    • (Barrett, A. J., Rawlings, N. D. and Woessner, J. F., eds). Academic Press, San Diego
    • Seidah N. G. and Chretien M. (1998b) Proprotein Convertase I, in Handbook of Proteolytic Enzymes (Barrett, A. J., Rawlings, N. D. and Woessner, J. F., eds), pp. 349-353. Academic Press, San Diego.
    • (1998) Handbook of Proteolytic Enzymes , pp. 349-353
    • Seidah, N.G.1    Chretien, M.2
  • 39
    • 0030937084 scopus 로고    scopus 로고
    • Proteolytic processing of pro-opiomelanocortin occurs in acidifying secretory granules of AtT-20 cells
    • Tanaka S., Yora T., Nakayama K., Inoue K. and Kurosumi K. (1997) Proteolytic processing of pro-opiomelanocortin occurs in acidifying secretory granules of AtT-20 cells. J. Histochem. Cytochem. 45, 425-436.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 425-436
    • Tanaka, S.1    Yora, T.2    Nakayama, K.3    Inoue, K.4    Kurosumi, K.5
  • 40
    • 0037307816 scopus 로고    scopus 로고
    • Advances in quantitative proteomics via stable isotope tagging and mass spectrometry
    • Tao W. A. and Aebersold R. (2003) Advances in quantitative proteomics via stable isotope tagging and mass spectrometry. Curr. Opin. Biotechnol. 14, 110-118.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 110-118
    • Tao, W.A.1    Aebersold, R.2
  • 41
    • 0035238444 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry: An elegant tool for peptidomics
    • Verhaert P., Uttenweiler-Joseph S., de Vries M., Loboda A., Ens W. and Standing K. G. (2001) Matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry: an elegant tool for peptidomics. Proteomics 1, 118-131.
    • (2001) Proteomics , vol.1 , pp. 118-131
    • Verhaert, P.1    Uttenweiler-Joseph, S.2    De Vries, M.3    Loboda, A.4    Ens, W.5    Standing, K.G.6
  • 43
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou A., Webb G., Zhu X. and Steiner D. F. (1999) Proteolytic processing in the secretory pathway. J. Biol. Chem. 274, 20745-20748.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 44
    • 0036428393 scopus 로고    scopus 로고
    • Amino acid residue specific stable isotope labeling for quantitative proteomics
    • Zhu H., Pan S., Gu S., Bradbury E. M. and Chen X. (2002) Amino acid residue specific stable isotope labeling for quantitative proteomics. Rapid Commun. Mass Spectrom. 16, 2115-2123.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 2115-2123
    • Zhu, H.1    Pan, S.2    Gu, S.3    Bradbury, E.M.4    Chen, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.